accession stringlengths 6 10 | name stringlengths 6 11 | Full Name stringlengths 1 147 ⌀ | taxon stringlengths 3 46 ⌀ | sequence stringlengths 16 2.75k | function stringlengths 6 5.51k | AlphaFoldDB stringlengths 6 10 |
|---|---|---|---|---|---|---|
Q8VHL0 | UT1_MOUSE | Urea transporter, erythrocyte | Mus | MEDSPTMVKVDRGENQILSCRGRRCGFKVLGYVTGDMKEFANWLKDKPVVLQFMDWILRGISQVVFVSNPISGILILVGLLVQNPWWALCGCVGTVVSTLTALLLSQDRSAIAAGLQGYNATLVGILMAVFSNKGDYFWWLIFPVSAMSMTCPVFSSALSSVLSKWDLPVFTLPFNMALSMYLSATGHYNTFFPSKLFTPVSSVPNITWSELSALELLKSLPVGVGQIYGCDNPWTGGIFLCAILLSSPLMCLHAAIGSLLGVIAGLSLAAPFEDIYFGLWGFNSSLACIAIGGMFMALTWQTHLLALACALFTAYFGAC... | Mediates the transport of urea driven by a concentration gradient across the cell membranes of erythrocytes and the renal inner medullary collecting duct which is critical to the urinary concentrating mechanism . Facilitates water transport in erythrocytes . | Q8VHL0 |
Q7VC41 | TPIS_PROMA | Triose-phosphate isomerase | Prochlorococcus | MRKTVIAGNWKMHMTCSSAKEYIDKFIPFSKEFPSDRHVVIAPPFTAISTLASLLQGTNIQLSSQNVHWEDTGAFTAEISPSMLLEHDVRYAIVGHSEPRKYFSESDEQINLRARSAQSNGLIPIVCVGESIEQRERGEAERVIRRQVEQGLEQTDLTKLVIAYEPIWAIGTGKTCESNEANRICGLIREWAGFSDLIIQYGGSVKPANIDEIMSMSDIDGVLVGGASLDPENFARIANYQSI | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q7VC41 |
Q8U4A5 | VATB_PYRFU | V-ATPase subunit B | Pyrococcus | MAKEYSTISRIYGPLMIVEGVKGVAYGEVVEIETEWGEKRKGQVLDARENLAIVQVFEGTRDLDIKTTRVRFTGETLKVPVSMDMLGRIFNGIGKPIDGGPEIIPEDRRDVHGAPLNPVARAYPRDFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNKLAAQIARQAKVLGEEESFAVVFAAMGITYEEANFFKKSFEETGAIERAVLFLNLADDPAIERIITPRMALTVAEYLAFDYDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVRGKKGSITQMPILTMPDDDITHPIPDLTG... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit. | Q8U4A5 |
Q9VZI3 | UN112_DROME | Fermitin-1 | Sophophora | MIHVGENTWNLRILITDLQVEKTLRVKGDQHIGGVMLNLVDPELPKDWSDHALWWPAKNIWLTRTRSTLDQAGVQSDSFLHFTPMHKTLRVQMPDLRYLDYRVNFSAKTFGAVVSLCKDLDIRYPEELSFCKPLEPEHLKKNFSKLPQRKIPVAEANGIAYVQPALDTNSFVPITGAYNGSNGSLDRSHNGNLLCAPASPYTRRAATAPGTPISSPTGTWKHNSTGYASYDSNSSFGDLQENLAMSPRSPSPDVRARLVRPKSRVEKARLNVGWLDSSLSIMEQGVREYDTLCLRFKYFTFFDLNPKYDQVRINQLYEQA... | Probably involved in cell adhesion. | Q9VZI3 |
Q9LKN0 | CHMO_ATRHO | Choline monooxygenase, chloroplastic | Atriplex | MAASATTMLLKYPTTVCGIPNSSANNSTDPSNNIVQIPQTTTTNSPLLKFRTPNKPVNAVAAPAFPSVTTTTTTTPSSIQSLVKDFDPLVPAEDALTPPSSWYTEPAFYAHELDRIFYKGWQVAGYSDQVKEANQYFTGTLGNVEYLVCRDGEGKVHAFHNVCTHRASILACGSGKKSCFVCPYHGWVYGMNGSLTKASKATPEQSLNPDELGLVPLKVAVWGPFILISLDRSSREVGDVGSEWLGSCAEDVKAHAFDPNLQFINRSEFPIESNWKIFSDNYLDSSYHVPYAHKYYATELDFDTYQTDMVGNVTIQRVAG... | Catalyzes the first step of the osmoprotectant glycine betaine synthesis. | Q9LKN0 |
Q4JAI6 | PCNA1_SULAC | Proliferating cell nuclear antigen homolog 1 | Sulfolobus | MRIVYDDVRDLKNIVETLTKFIDEGLFEIGQDGIRLVAVDKAHVSLINIELYKELFKEYEVEDEFKFGFNSQYLAKILSIAKRKEEISIESDSPERVKITLGGALNRVFIINNIQVSPPEVPEVNLEFEVKASLSSKAFKTTINEISAVTDTVDIIAVEDKVILKGEGKEGSQIENEFSKDTGAISDMEFKNEAKSPYDVNYLSDILSLTNLSDYTRLAFSTEKPLELEFNMEGGGKVTYLLAPKLS | Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication. | Q4JAI6 |
A9WKM8 | METXA_CHLAA | Homoserine transacetylase | Chloroflexus | MEAIVQAPTPEGVGIVRTQRMHWTTPLTLTSGATLGPITLAYETYGELAPDRSNAILILHALSGDAHAAGFHSPTDRKPGWWDAMIGPGRPFDTNRYFVICSNVIGGCRGSTGPSSPHPSDGRPYGSRFPLITIEDMVHAQQRLIDALGIDTLLAVAGGSMGGFQALAWTVEYPQRVRGAILLATSARSSPQTVAWNYIGRRAIMADPRWRGGDYYDSDAPRDGLAVARMLGHITYLCEEKLEQRFGRRVDGDALDLGPRFAIEHYLEHQAARFNDRFDANSYLVITRAMDNWDLTARYGSLTAAFDLTRARFLALAYSS... | Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. | A9WKM8 |
A1TVP2 | 1A1D_ACIAC | 1-aminocyclopropane-1-carboxylate deaminase | Acidovorax | MNLQKFPRHALTFGPTPIHPLKRLSAHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLIPEAIEGGYDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIEMSRIMGADVRLDAAGFDIGIRPSWEQAMEDVRRAGGKPFPIPAGCSEHPRGGLGFVAFAEEVRQQEEELGFQFDYIVVCSVTGSTQAGMVVGFAADGRADRVIGIDASAKPEQTREQILRIARNTAELVELGREITDADVVLDTRYGGPEYGLPNEGTLEAIRLCARQEGMLTDPVYEGKSMHGMIDMVRNGEFPAGSRVLYA... | Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. | A1TVP2 |
Q9CWH1 | ZBT8A_MOUSE | Zinc finger and BTB domain-containing protein 8A | Mus | MEISSHQSYLLQQLNEQRRQDVFCDCSILVEGKVFKAHRNVLFASSGYFKMLLSQNSRETSQPTTATFQTFSPDTFTVILDFVYSGKLSLTGQNVIEVMSAASFLQMTDVISVCKTFIKSSLDISEKEKDRYFSLSDKDTGSNGVERPPFYSSSWQEEGGSPHSHVSPDPGKPWNKYGYPPASQRSPQRPLAKHEQRKEPSKKAKHVRLPQPSEVVHFKPGKGEAQTDSGNHVSQSEEQVPVDAEVDPAPAGFQYSQGPDGIARSFPDDLTRLRFKCPFCTHVVKRKADLKRHLRCHTGERPYPCQACGKRFSRLDHLSS... | May be involved in transcriptional regulation. | Q9CWH1 |
Q63DG7 | XPT_BACCZ | Xanthine phosphoribosyltransferase | Bacillus cereus group | MKVLQEKILNEGKVLSGDVLKVDAFLNHQIDPVLMQEIGKEFAKRFKEENITKIVTIESSGIAPAVMAALELGVKVIFARKRKSLTLQDNMYVASVYSFTKQETNEISLSRNHIDESDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQDGGKKLREQGIRVESLAEIASLDNNAVTFVQQETAEVK | Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. | Q63DG7 |
Q3MFR5 | CLPP1_TRIV2 | Endopeptidase Clp 1 | Trichormus | MTIPIVIEQSGRGERAFDIYSRLLRERIIFLGQQVDSNLANLIVAQLLFLDAEDPEKDIYLYINSPGGSVTAGMGIFDTMKHIRPDVCTICTGLAASMGAFLLSAGTKGKRMSLPHSRIMIHQPLGGAQGQATDIEIQAREILYHKRRLNDYLAEHTGQPIERIAEDTERDFFMSPDEARDYGLIDQVIDRHAAGSRPVAMVNQ | Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. | Q3MFR5 |
Q1IGC6 | METXS_PSEE4 | Homoserine transsuccinylase | Pseudomonas | MSTVLPEDSVGLVTPQIARFDEPLALACGRSLAAYELIYETYGELNASASNAVLICHALSGHHHAAGYHAATDRKPGWWDSCIGPGKPIDTNRFFVVSLNNLGGCNGSTGPSSVNPATGKPYGADFPVLTVEDWVHSQARLADRLGIQTWAAIVGGSLGGMQALQWTITYPDRVRHCVDIASAPKLSAQNIAFNEVARQAILTDPEFHGGSFQDQGVTPKRGLMLARMVGHITYLSDDSMGEKFGRELKSDKLNYDFHSVEFQVESYLRYQGEEFSGRFDANTYLLMTKALDYYDPAAAHGGDLAATLAHVTADYCIMSF... | Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. | Q1IGC6 |
Q8TSY1 | RNFE_METAC | Rnf electron transport complex subunit E | Methanosarcina | MYPHRRADMNPISEFIRGITKDNPTFGLVLGLCPTLAVTTSVENGIGMAMGTLFVLVGSNMMVSAIRKGIPGTVRLPVEIIVIATFVTIVDMVMEAFTPDLYTSLGVFIPLIVVNCIVIGRAEAYALKNGVFYSIIDALGEGTGFLLVLILIGGIRELLGTGIIDPFGMTLINLSGVINPAMFMTMSPGAFLTIAVLMTIVNYRRQQKAAKGG | Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Catalyzes Na(+) transport, most probably coupled to electron transfer from reduced ferredoxin to methanophenazine and heterodisulfide reductase. Involved in heterodisulfide reduction during methanogenesis fro... | Q8TSY1 |
Q9UPW5 | CBPC1_HUMAN | Protein deglutamylase CCP1 | Homo | MSKLKVIPEKSLTNNSRIVGLLAQLEKINAEPSESDTARYVTSKILHLAQSQEKTRREMTAKGSTGMEILLSTLENTKDLQTTLNILSILVELVSAGGGRRVSFLVTKGGSQILLQLLMNASKESPPHEDLMVQIHSILAKIGPKDKKFGVKARINGALNITLNLVKQNLQNHRLVLPCLQLLRVYSANSVNSVSLGKNGVVELMFKIIGPFSKKNSSLIKVALDTLAALLKSKTNARRAVDRGYVQVLLTIYVDWHRHDNRHRNMLIRKGILQSLKSVTNIKLGRKAFIDANGMKILYNTSQECLAVRTLDPLVNTSSL... | Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins . Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin . Specifically cleaves tubulin long-side-chains, w... | Q9UPW5 |
Q8VEB3 | MACIR_MOUSE | Macrophage immunometabolism regulator | Mus | MEVDINGDSRSTLTTLPLPVAEGSSPGKAEAEKPRCSSTPCSPMRRTVSGYQILHMDSNYLVGFTTGEELLKLAQKCTGGEDSKGEAMPALRAKQLDTGLARSSRLYKTRSRYYQPYEIPAVNGRRRRRMPSSGDKCTKPLPYEPYKALHGPLPLCLLKGKRAHSKSLDYLNLDKMNIKEPADTEVLQYQLQHLTLRGDRVFARNNT | Regulates the macrophage function, by enhancing the resolution of inflammation and wound repair functions mediated by M2 macrophages. The regulation of macrophage function is, due at least in part, to its ability to inhibit glycolysis. May also play a role in trafficking of proteins via its interaction with UNC119 and ... | Q8VEB3 |
P93655 | LONM1_ARATH | Lon protease homolog 1, mitochondrial | Arabidopsis | MLKLFTSSASRVHHLTPVSRVVGSSPVESPLFKALSQITGWNRRSTSLGHRAFFCSEPTNGEAAAEAETKAVESDSEVSDSKSSSAIVPTNPRPEDCLTVLALPVPHRPLFPGFYMPIYVKDPKVLAALQESRRRQAPYAGAFLLKDDPSADSSSSTDAEKNINELKGKELLNRLHEVGTLAQISSIQGDQVILVGHRRLRIKEMVSEEPLTVKVDHLKDNPFDMDDDVVKATSFEVISTLRDVLKTSSLWRDHVQTYTQHIGDFTYPRLADFGAAICGANRHQAQEVLEELDVHKRLRLTLELMKKEMEISKIQETIAK... | ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the ... | P93655 |
Q9B5Q1 | CYB_SYLGR | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Sylvicapra | MTNIRKTHPLLKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTADTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHVGRGLYYGSYAYTETWNIGVILLFATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFIFPFIIAALAMVHLLFLHETGSNNPTGISSDADKIPFHPYYTIKDILGVLLLILALMTLVLFSPDLLGDPDNYPPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILILMPLLHTSKQRSMMFRPI... | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is... | Q9B5Q1 |
Q8L9K1 | ERF99_ARATH | Ethylene-responsive element-binding factor 13 | Arabidopsis | MSSSDSVNNGVNSRMYFRNPSFSNVILNDNWSDLPLSVDDSQDMAIYNTLRDAVSSGWTPSVPPVTSPAEENKPPATKASGSHAPRQKGMQYRGVRRRPWGKFAAEIRDPKKNGARVWLGTYETPEDAAVAYDRAAFQLRGSKAKLNFPHLIGSCKYEPVRIRPRRRSPEPSVSDQLTSEQKRESHVDDGESSLVVPELDFTVDQFYFDGSLLMDQSECSYSDNRI | Acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. Involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways. | Q8L9K1 |
Q9ZT17 | AGP3_ARATH | Classical arabinogalactan protein 3 | Arabidopsis | MALKTLQALIFLGLFAASCLAQAPAPAPITFLPPVESPSPVVTPTAEPPAPVASPPIPANEPTPVPTTPPTVSPPTTSPTTSPVASPPKPYALAPGPSGPTPAPAPAPRADGPVADSALTNKAFLVSTVIAGALYAVLA | Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death. | Q9ZT17 |
C1DQA8 | SECA_AZOVD | Protein translocase subunit SecA | Azotobacter | MFAPLLRVLFGSKNDREVKRMRRAVRAINALEEQMVALTDEQLRAKTEEFRGRLGKGETLDQLLPEAFAVAREAGKRVMGMRHFDVQLIGGMVLHEGKIAEMRTGEGKTLVATLAVYLNALAGKGVHVVTVNDYLARRDANWMRPLYEFLGLSVGVVTPFQPPEEKRAAYAADITYGTNNEFGFDYLRDNMAFSLEDKFQRELNYAVIDEVDSILIDEARTPLIISGQAEDSSQLYLQINALIPRLKRHIEEEEGVVTQEGHYVVDEKTRQIELNEQGHQFIEELLASAGLLPEGDNLYSAHNLQLLTHVYAGLRAHVLF... | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor drivin... | C1DQA8 |
P53591 | SUCD_COXBU | Succinyl-CoA synthetase subunit alpha | Coxiella | MSILIDKETRVLCQGFTGKQGTFHSEQAIEYGTQMVGGVTPGKGGQSHLGLPIFNSVHEAVEETSADATMIFVPAPFCKDSIIEAVDAGVRLVVCITEGIPVLDMLEVKAYLRQHPDVRMIGPNCPGVITPGECKIGIMPGHIHQRGKVGIVSRSGTLTYEAVNQTTQMGFGQSTCVGIGGDPIPGTSFIDVLEMFEKDSQTQAIVMVGEIGGTAEEEAAEFIQSNVKKPVISYIAGVTAPPGKRMGHAGAIIAGGKGTAADKYAALEAAGVFVVKSPAEIGKGVAEATGWSTH | Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate ... | P53591 |
P0AA83 | CODB_ECOL6 | Cytosine permease | Escherichia | MSQDNNFSQGPVPQSARKGVLALTFVMLGLTFFSASMWTGGTLGTGLSYHDFFLAVLIGNLLLGIYTSFLGYIGAKTGLTTHLLARFSFGVKGSWLPSLLLGGTQVGWFGVGVAMFAIPVGKATGLDINLLIAVSGLLMTVTVFFGISALTVLSVIAVPAIACLGGYSVWLAVNGMGGLDALKAVVPAQPLDFNVALALVVGSFISAGTLTADFVRFGRNAKLAVLVAMVAFFLGNSLMFIFGAAGAAALGMADISDVMIAQGLLLPAIVVLGLNIWTTNDNALYASGLGFANITGMSSKTLSVINGIIGTVCALWLYNN... | Required for cytosine transport into the cell. | P0AA83 |
C1DCA5 | NUOC_LARHH | NDH-1 subunit C | Laribacter | MASSLDALKARVESLLGDHLESATIDRGELTIVCSASSIAVSCQLLRDQAGFDQCIDLCGMDYSTYRDGLHDRPRFAVVLHLMSVQNNQRLRVRFFAPDDDFPVVPSLIDVWASVNWYEREAFDMYGIVFEGHPDLRRILTDYGFVGHPFRKDFPVSGHVEMRYDPTEGRVIYQPVTIEPREITPRIIREENYGG | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are t... | C1DCA5 |
Q2NUV8 | LIPA_SODGM | Sulfur insertion protein LipA | Sodalis | MSKPIQMERGVKYRDADKMALIPIKTVAVERQEILRKPSWMKIKLPADSTRIQGIKVAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVTPDANEPEKLAQTIADMGLRYVVVTSVDRDDLRDGGAQHFADCISAIRAKNPNIRIETLVPDFRGRMDRALEIINAAPPDVFNHNLENVPRLYRQVRPGADYHWSLKLLENFKVANPQLPTKSGLMVGLGETNAEIVDVMRDLCRHGVTMLTLGQYLQPSRHHLPVKRYVSPQEFDEMKQEALAMGFTHAACGPFVRSSYHADLQAKGIEV... | Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | Q2NUV8 |
Q0AUC8 | ATPL_SYNWW | Lipid-binding protein | Syntrophomonas | MGVALGAGLAVSIAGIGGGIGMGIAGGKAFEAIARQPEVGGDVRTLLFITLAFIETLTIYGLLIAFMLVGKA | Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. | Q0AUC8 |
B5Y1T9 | SECA_KLEP3 | Protein translocase subunit SecA | Klebsiella | MLIKMLTKVFGSRNDRTLRRMRKVVNIINGMEPAMEKLSDDELKAKTAEFRARLEKGEVLENLIPEAFAVVREASKRVFGMRHFDVQLLGGMVLNDRCIAEMRTGEGKTLTATLPAYLNALTGKGVHVVTVNDYLAQRDAENNRPLFEFLGMSVGINMSGLPAPAKREAYAADITYGTNNEYGFDYLRDNMAFSPEERVQRKLHYALVDEVDSILIDEARTPLIISGPAEDSSEMYRKVNKIIPHLIRQEKEDSDTFTGEGHFSVDEKARQVNLTERGLVLIEELLVQEGIMEEGESLYSPTNIMLMHHVTAALRAHALF... | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor drivin... | B5Y1T9 |
Q6FYZ6 | GCSH_BARQU | Glycine cleavage system H protein | Bartonella | MSQIYFTQDHEWLSVEGQVVTVGITNYAQEQLGDLVFVDLPQSGTKLSKGDAAAVVESVKAASDVYAPLDGEVVEINEALANSPELVNQKAEKEGWLWKMTVQDETQLEGLLDEAAYKTLIG | The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | Q6FYZ6 |
A6KYS6 | LUXS_PHOV8 | Autoinducer-2 production protein LuxS | Phocaeicola | MKTIPSFTIDHIRLLRGIYVSRKDEVGGETVTTFDIRMKEPNREPALGQGALHTIEHLAATYLRNHPIWSDKIVYWGPMGCLTGNYLLMKGDLKSEDIVELMQETFRFVADFEGEVPGAAPKDCGNYLLHDLPMAKWESAKYLHEVLEHMTKDNLYYPTKE | Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhom... | A6KYS6 |
A4SVI8 | KAD_POLAQ | Adenylate monophosphate kinase | Polynucleobacter | MRLILLGAPGAGKGTQAQFICEKFAIPQISTGDMLRAAVKAGTEFGVAAKKIMDAGGLVSDDIIIGLVKDRLTQPDCSKGYLFDGFPRTIPQAQAMKDAGVPIDYVLEIDVPFDAIIDRMGGRRVHPASGRTYHIKYNPPKVEGKDDVTGDALIQRDDDKEETVRKRLQVYDDQTRPLVEYYSSWAAQANAADKVKAPAYRKVSGTGSVEDITTSIFAQLK | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | A4SVI8 |
A7FUX9 | MSRA_CLOB1 | Peptide-methionine (S)-S-oxide reductase | Clostridium | MKEIVLAGGCFWGVEEYMSRIEGIVETKVGYANGIKENPSYEEVCSGVTGHAEACYIKYDESIISLEELLNKFWSIIDPTVLNKQGNDRGTQYRTGIFYLDEKDLNVIIKSKYQEQKNYRKPIVTEVEPLKCFYEAEEYHQKYLKKNPGGYCHIHLD | Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | A7FUX9 |
Q6G1A4 | PURA_BARQU | IMP--aspartate ligase | Bartonella | MANVVVVGTQWGDEGKGKIVDWLSERADIVVRYQGGHNAGHTLVVNGVNYKLSLLPSGLVRGKLSIIGNGVVVDPHHFVAELKKLRDQGVKITPEILRIAENAPLILSLHRDLDATRESGLSGLKIGTTKRGIGPAYEDKVGRRAIRVMDLAETNTLMAKIERLLAHHNALRRGMGVAEINSQALYDELMQVADEILPFMDCTWRLLDESYQVGKHVLFEGAQGALLDNDFGTYPYVTSSNTVAGQACTGSGIGPGVIHYVLGIAKAYTTRVGEGPFPTEQINDIGEFLGMRGKEFGVVTGRKRRCGWFDAVLVRQMVTI... | Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. | Q6G1A4 |
Q5X4B2 | MUTS_LEGPA | DNA mismatch repair protein MutS | Legionella | MSSSHTPMMQQYLRIKTDYPDMLLFYRMGDFYELFFDDAKRASQLLDLTLTHRGQSADKPIPMAGVPYHAVENYLARLLKKGESVAICEQIGDPATSKGPVERQVTRIITPGTVTDEALLDARKDNILLAIHTQKQKIGIAWVDLGGGRFHLQELTEEHQLNAELVRLQPAELLCKESTPLPSFCSNFAVKFRPGWEFDASNAHKLLCEQFSVTDLSAFGEQNYPTALIAAGALLAYLKTTQKQSLPHLTTLTLEQSEDYLQLDASTQKHLELFENIHGGGEHCLLSILDKTACAMGSRLLKRWLGKPLKQHAIIQTRQQ... | This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | Q5X4B2 |
Q3YUK4 | DSBD_SHISS | Protein-disulfide reductase | Shigella | MAQRIFTLILLLCSTSVFAGLFDAPGRSHFVPADQAFAFDFQQNQHDLNLTWQIKDGYYLYRKQIRITPEHAKIADVQLPQGVWHEDEFYGKSEIYRDRLTLPVTINQASAGATLTVTYQGCADAGFCYPPETKTVPLSEVVANNAASQPVSVPQQEQHTAQLPFSALWALLIGIGIAFTPCVLPMYPLISGIVLGGKQRLSTARALLLTFIYVQGMALTYTALGLVVAAAGLQFQAALQHPYVLIGLAIVFTLLAMSMFGLFTLQLPSSLQTHLTLMSNRQQGGSPGGVFVMGAIAGLICSPCTTAPLSAILLYIAQSG... | Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. | Q3YUK4 |
Q5XC65 | GLYA_STRP6 | Serine hydroxymethyltransferase | Streptococcus | MIFDKGNVEDFDKELWDAIHAEEERQEHHIELIASENMVSKAVMAAQGSVLTNKYAEGYPGNRYYGGTECVDIVETLAIERAKKLFGAAFANVQAHSGSQANAAAYMALIEAGDTVLGMDLAAGGHLTHGSPVNFSGKTYHFVGYSVDADTEMLNYEAILEQAKAVQPKLIVAGASAYSRSIDFEKFRAIADHVGAYLMVDMAHIAGLVAAGVHPSPVPYAHIVTSTTHKTLRGPRGGLILTNDEALAKKINSAVFPGLQGGPLEHVIAAKAVAFKEALDPAFKDYAQAIIDNTAAMAAVFAQDDRFRLISGGTDNHVFL... | Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent a... | Q5XC65 |
B8G5S6 | RUVB_CHLAD | Holliday junction ATP-dependent DNA helicase RuvB | Chloroflexus | MSAERLVNPHSDSDDQQVEKSLRPRTLSEFIGQEKVVEQLRIAIAAARGRNEALDHTLFYGPPGLGKTSLANVVANEMGAKIKITSGPAIERAGDLAAILTNLQPNDVLFIDEVHRLNRAVEEVLYPAMEDFALDLVVGKGPGARSLRLNLPRFTVIGATTRLALLTSPLRDRFVAVHRLVFYSDAAMTEIVSRSARILGVPISPEGAREIGRRARGTPRIANRILRRVRDYAQVVANGEITLAVAREALAQLEIDELGLDENDRRLLRAIIELFNGGPVGLNTLAAALAEEVDAIEDVYEPFLLQLGFLQRTPRGRVAT... | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. | B8G5S6 |
A3QCG6 | DER_SHELP | GTP-binding protein EngA | Shewanella | MIPVVALVGRPNVGKSTLFNRLTRTRDALVADYPGLTRDRKYGRAHLSGYEFIVVDTGGIDGTEEGIETRMAEQSLAAIEEADVVLFLTDARAGLTAADEAIAEHLRRREKTTFVVANKVDGIDADSACGEFWALGLGEVYQMAAAQGRGVTNMIEYALTPYAEAMGLTRDGEGEEEADERQYTEEEAEAEQQRLQDLPIKLAIIGKPNVGKSTLTNRILGEERVVVYDEPGTTRDSIYIPLERDGQEYVIIDTAGVRRRSKVHETVEKFSVIKTLKAVEDANVVLLVVDAREGIAEQDLGLLGFALNVGRALVIAVNKW... | GTPase that plays an essential role in the late steps of ribosome biogenesis. | A3QCG6 |
Q1H4M0 | RS5_METFK | 30S ribosomal protein S5 | Methylobacillus | MAKVEIEQQQTDGLREKMIGVNRVTKVVKGGRIMSFAALSVVGDGDGGVGMGKGKAREVPVAVQKAMDEARRSMIKVSLNNGTLYHAVTGVHGAAKVFIQPASEGTGIIAGGAMRAIFEVMGVTNVLAKCIGSTNPYNVVRATLNGLKSMNTPAEIAAKRGKSVEEIRG | Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. | Q1H4M0 |
H2A0N4 | PIF_PINMG | Aragonite-binding protein | Pinctada | MQVPYLQIVFLLTAVFGIGVKSDDCKTADLVVNVDGSDDVSDREFDKLKRAMLMLVRGLSIDDSQIRLGMVTYGSEIGDSIPLQGDRLDLARTIRYMKKPGGPCKPFKGIGETRKMFSSRGRFNVPHVTLNLGGDIVDSEVRDLMDETDKARDEDIKVMAIGLGTKVERDEIEGIAWDKEQAYFMDDADDLVRRVKEIPDYLCKIIKAKKPRKSASKKSKTKPAKKPDSDIVGKSPGFHSLQRTDDKPKMSKKVEVKELCDDAEWVEDVGYGSVPTRCEDFVMCQNVSGSLRKTLKTCPYGQFWSRARTSCVLTEDEDCS... | Pif97 contains a chitin-binding domain that allows for attachment of the entire complex to the chitin-containing organic framework. | H2A0N4 |
Q49KY5 | CYF_EUCGG | Cytochrome f | Eucalyptus | MQTKNTFSWIKKEIIRSISVSLMIYIIARTSISNAYPIFAQQGYENPREATGRIVCANCHLANKPVDIEVPQAVLPDTVFEAVVRIPYDMQVKQVLANGKRGGLNVGAVLILPEGFELAPPDRISPEMKEKIGNLSFQSYRPNKKNILVIGPVSGQKYSEVTFPILSPDPATNKDVHFLKYPIYVGGNRGRGQIYPDGSKSNNTVYNATAAGVVSKIIRKEKGGYEITISDASDERQVVDIIPPGPELLVSEGESIKLDQPLTSNPNVGGFGQGDAEIVLQDPFRVQGLLFFLASVILAQIFLVLKKKQFEKVQLSEMNF | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | Q49KY5 |
Q5WWT0 | SERC_LEGPL | Phosphohydroxythreonine aminotransferase | Legionella | MNSRVFNFGAGPAMLPEEILKEAQEEFLNWRNTGMSILEIGHRTPEIISLLSTAEQSLRELLNIPKNYHVLFLGGAARTQFAMIPMNLLRPGDDAAYFITGIWSKMAYHEANLLKKAYYLSSEEKEGFVSIPDYQKWELKSNTAYVYYTPNETINGVRFPYVPKTGGVPLVADMTSCLLSEPININQYGLIFAGAQKNIANAGLTVVIIHEELLKNQPEPVIPTMLNYKNHAEHRSLYATPPVFNCYLASKMFEWIKTQGGIEGLFQRNCLKAAKLYQYLDSTDFYLTPVFKEARSIMNICFSLCYPDLEHKFLDMANER... | Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine. | Q5WWT0 |
A6MVX4 | RPOB_RHDSA | Plastid-encoded RNA polymerase subunit beta | Rhodomonas | MSSTKLSTSILPDLVEIQRASFCWFLEEGLAEEIKSFSPITDYTGNLELHFFGDQFKLKCPKYNLLESKRRDATYSVQVYVPARLINRDTGIIKEQEVFIGDLPLMTDRGTFIINGAERVIVNQIVRSPGIYYKSETDRQGRRTYSGSLISNRGAWVKFETDRNDLVWVRIDKTRKIPAHVFLKAMGLSDSDIYNGLRHPEYLKKSFRVEGNYTTEEALIQMYTKLRPGEPATVNGGQQILYSRFFDPKRYDLGKVGRYKINKKLALSIPENIKVLTPQDTLSAIDYLINLKFNIGETDDIDHLGNRRVRSVGELLQNQV... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A6MVX4 |
A7I3D6 | FABH_CAMHC | 3-oxoacyl-[acyl-carrier-protein] synthase III | Campylobacter | MKNAAMLSIGAYVPPYELSNFDLEKMVETSDEWIVKRTGIHTRHIAKNETAGDMAAKAADLAISRSGISKEEIDAIICATITPDFFCMPSTACITAEKLGLNKGITAFDISAACSGFIYLLEIGSALIKSGAKKNVLIIGTEKLSSIVDWKDRATCVLFGDGAGAAVLSCMDNKNNGISKPYGIIDIHTASDGNKAELLMTPTKNSNIKDIADENLGFLHMKGNEVFKIAVQTLSNDVVKILKKNNVKPEEIDLFVPHQANFRIIEAVKNRLNFTDNQCVVTVGKYGNTSSASIPIALNEAYENGRLKNGSLILLDAFGG... | Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-A... | A7I3D6 |
Q4R3Q1 | IF4A3_MACFA | Eukaryotic initiation factor 4A-III, N-terminally processed | Macaca | MATTATMATSGSARKRLLKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILAPARELAVQIQKGLLTLGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIM... | ATP-dependent RNA helicase. Involved in pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic a... | Q4R3Q1 |
B5BLB2 | LEUD_SALPK | Isopropylmalate isomerase | Salmonella | MAEKFTQHTGLVVPLDAANVDTDAIIPKQFLQKVTRTGFGAHLFNDWRFLDEKGQQPNPEFVLNFPEYQGASILLARENFGCGSSREHAPWALTDYGFKVVIAPSFADIFYGNSFNNQLLPVKLSDEQVDELFTLVKANPGIKFEVDLEAQVVKAGDKTYSFKIDDFRRHCMLNGLDSIGLTLQHEDAIAEYENKQPAFMR | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | B5BLB2 |
Q8NBR6 | MINY2_HUMAN | Protein FAM63B | Homo | MESSPESLQPLEHGVAAGPASGTGSSQEGLQETRLAAGDGPGVWAAETSGGNGLGAAAARRSLPDSASPAGSPEVPGPCSSSAGLDLKDSGLESPAAAEAPLRGQYKVTASPETAVAGVGHELGTAGDAGARPDLAGTCQAELTAAGSEEPSSAGGLSSSCSDPSPPGESPSLDSLESFSNLHSFPSSCEFNSEEGAENRVPEEEEGAAVLPGAVPLCKEEEGEETAQVLAASKERFPGQSVYHIKWIQWKEENTPIITQNENGPCPLLAILNVLLLAWKVKLPPMMEIITAEQLMEYLGDYMLDAKPKEISEIQRLNYE... | Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins . Binds to polyubiquitin chains of different linkage types, including 'Lys-6', 'Lys-11', 'Lys-29', 'Lys-33', 'Lys-48' and 'Lys-63' . May play a regulatory role at the level of protein turnover . | Q8NBR6 |
L0T905 | RSEA_MYCTU | Sigma-E anti-sigma factor RseA | Mycobacterium tuberculosis complex | MADPGSVGHVFRRAFSWLPAQFASQSDAPVGAPRQFRSTEHLSIEAIAAFVDGELRMNAHLRAAHHLSLCAQCAAEVDDQSRARAALRDSHPIRIPSTLLGLLSEIPRCPPEGPSKGSSGGSSQGPPDGAAAGFGDRFADGDGGNRGRQSRVRR | An anti-sigma factor for extracytoplasmic function (ECF) sigma factor SigE. ECF sigma factors are held in an inactive form by an anti-sigma factor. | L0T905 |
B7GZQ9 | QUEF_ACIB3 | PreQ(0) reductase | Acinetobacter calcoaceticus/baumannii complex | MSVEQSLLGKETQYPTSYQPDVLFPIARAQSREKYAHIQGITQGKDWWHVFEISWLNAHGIPQVAIGRITLPASSPNLIESKSLKLYFNSLNFTQFDSTQSFIETVEKDLSAAAGAKVELTLFQVDDLEISKPQGICIDDLMPERLEQHPDATLLKLDESGEEIEVELYSHLLRSNCPVTGQPDWGTVFIRFKGKKPCYRSLLAYIISYRQHNGFHEQCVEQIFADIWQNLQPEKLMVYATYTRRGGLDINPCRVSDLTWMPKPIRLARQ | Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). | B7GZQ9 |
A4WQD9 | DDL_CERS5 | D-alanylalanine synthetase | Cereibacter | MAGRSGRTFPRVAVLMGGTSSEREVSLSSGHSCSAALRDAGYEVTEVDAGPDLARVLAEVQPDAVFNALHGRWGEDGCVQGLLEWLRIPYTHSGVLASALAMDKARAKEVFAAAGLPVTQSVIATPDEVQAGHVLPPPYVVKPNCEGSSVGVYIVQADANGPPRLAPDMPRDLMVETYIPGRELTVTVMGDRALAVTDIVTDGWYDYDAKYRPGGSRHVVPAELPAEITDACLDIALRAHRALGCRGISRSDLRWDESRGAEGLILLETNTQPGMTPTSLSPEQAAHCGLSFPEFCAWMVEDASCNR | Cell wall formation. | A4WQD9 |
Q7VUH1 | KPRS_BORPE | Phosphoribosyl pyrophosphate synthase | Bordetella | MIFTGTANTRLAVDVVNHLDMSLGKMTVGRYSDGEVMVEINENVRGKDVFVLQPTCAPTNDNLMEIMVMVDALRRASAGRITAAIPYFGYARQDRRPRSARVAISAKVVANMLQVAGVDRVLTMDLHADQIQGFFDIPVDNIYAGPILLGDIWRRNFSNLVVVSPDIGGVVRARALAKQLEADLAIIDKRRPRANVSEVMNIIGEVDGRTCIIMDDMVDTAGTLCKAAQALKDRGAGAVYAYCTHPVLSGGAIERIETSSLDELVVTDTIPLSEQAQACGKIRQLSCAALLGETILRISNAESVSSLFAD | Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). | Q7VUH1 |
O25150 | CMOA_HELPY | Carboxy-S-adenosyl-L-methionine synthase | Helicobacter | MKDTLFNESLNKRFCFDEKVAHVFDDMLERSIPYYHEMLNLGAYFIAQNLKENIYPKSLPKPLIYDLGCSTGNFFIALNRQIQQEIELVGIDNSMPMLKKAQEKLKDFNNARFECMDFLEVEFKEASAFSLLFVLQFVRPMQREVLLKKIYNSLALNGVLLVGEKIMSEDRILDKQMIELYYLYKQNQGYSHNEIAFKREALENVLVPYSLKENVALLESVGFKHVEALFKWVNFTLLVARKT | Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM). | O25150 |
B9DPQ3 | PYRR_STACT | Uracil phosphoribosyltransferase | Staphylococcus | MSERIVLDEAAMKRTLMRMAHEILEYNRGTKDLVLLGVKTRGEFLAKSIQSKIQQIENTTVPTGTIDITQFRDDLELPTPKISEKSFVIDVDITDKVVIIIDDVLYTGRTVRASLDAILLHSRPQKIGLAALVDRGHRELPIRADFVGKNIPTARDEAVSVYVKETDGRNAVIIE | Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. | B9DPQ3 |
Q16674 | MIA_HUMAN | Melanoma inhibitory activity protein | Homo | MARSLVCLGVIILLSAFSGPGVRGGPMPKLADRKLCADQECSHPISMAVALQDYMAPDCRFLTIHRGQVVYVFSKLKGRGRLFWGGSVQGDYYGDLAARLGYFPSSIVREDQTLKPGKVDVKTDKWDFYCQ | Elicits growth inhibition on melanoma cells in vitro as well as some other neuroectodermal tumors, including gliomas. | Q16674 |
B1ZDN3 | LEU1_METPB | Alpha-isopropylmalate synthase | Methylorubrum | MANTTESAKDRVVIFDTTLRDGEQCPGATMTLDEKLAVAELLDAMGVDIIEAGFPIASNGDFEAVSEIARRTKRATIAGLARAIPADIARAGEAVRHAKAGRIHTFVSTSAIHLAHQMRKTQDEVIEIILKTVTQARDLVEDVEWSAMDATRTDIDYLCRCVEAAIRSGATTINLPDTVGYATPQEYGAMFRQVRERVPNSDKAIFSVHCHNDLGLAVANSLAGLEGGARQIECTVNGIGERAGNAALEEIVMAIRTRADVMPYDTGIDTTMLTRASKLVSHAANFPVQYNKAIVGRNAFAHESGIHQDGMLKHSETYEI... | Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). | B1ZDN3 |
P00852 | ATP6_EMEND | F-ATPase protein 6 | Aspergillus subgen. Nidulantes | MYQFNFILSPLDQFEIRDLFSLNANVLGNIHLSITNIGLYLSIGLLLTLGYHLLAANNKIIPNNWSISQEAIYATVHSIVINQLNPTKGQLYFPFIYALFIFILVNNLIGMVPYSFASTSHFILTFSMSFTIVLGATFLGLQRHGLKFFSLFVPSGCPLGLLPLLVLIEFISYLSRNVSLGLRLAANILSGHMLLSILSGFTYNIMTSGILFFFLGLIPLAFIIAFSGLELAIAFIQAQVFVVLTCSYIKDGLDLH | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous ca... | P00852 |
C6DF35 | ARGP_PECCP | HTH-type transcriptional regulator ArgP | Pectobacterium | MKRPDYRTLQALDAVIRERGFERAAQKLCITQSAVSQRIKQLENLFGQPLLVRTIPPRPTEQGQKLLALLHQVELLEEEWLGNETNSDIPLLLSLAVNADSLATWLLPALQPVLVDSPIRLNLQVEDETRTQERLRRGEVVGAVSIQSQPLPSCLVDKLGALDYLFVASPTFAARYFPNGVTRSALLRAPAVAFDHLDDMHQAFLQQNFDLSPGSVPCHIVNSSEAFVQLARQGTTCCMIPHLQIEKELANNELVDLTPGLFQRRMLYWHRFAPESRMMRKVTDALLAHGHQVLRQS | Controls the transcription of genes involved in arginine and lysine metabolism. | C6DF35 |
Q2QNM1 | MCM7_ORYSJ | Minichromosome maintenance protein 7 | Oryza sativa | MAATATKTIDFAAERALAKDFLANFAGPRGEPKYLNILQDVANRKIRAVQIELDDLFHYKDADDEFLQRVTENTKRYIGIFADAIDELMPESTEAYAVDEDRDILMTQRVDEGADGGADGTDPLQRMPPEIRRFFEVYIKAFSKVTPLTIRQVKASNIGQLVKISGIVTRCSDVKPLMQVAVYTCEECGFEIYQEVTARVFMPLFECPSQRCKLNKAKGNLILQLRASKFLKFQEVKLQELAEHVPKGHIPRSLTVHLRGELTRKVAPGDVVEMSGIFLPMPYYGFRAMRAGLVADTYLESMSITHFKKKYEEYELKGDE... | Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells. | Q2QNM1 |
Q96M32 | KAD7_HUMAN | ATP-AMP transphosphorylase 7 | Homo | MAEEEETAALTEKVIRTQRVFINLLDSYSSGNIGKFLSNCVVGASLEEITEEEEEEDENKSAMLEASSTKVKEGTFQIVGTLSKPDSPRPDFAVETYSAISREDLLMRLLECDVIIYNITESSQQMEEAIWAVSALSEEVSHFEKRKLFILLSTVMTWARSKALDPEDSEVPFTEEDYRRRKSHPNFLDHINAEKMVLKFGKKARKFAAYVVAAGLQYGAEGGMLHTFFKMAWLGEIPALPVFGDGTNVIPTIHVLDLAGVIQNVIDHVPKPHYLVAVDESVHTLEDIVKCISKNTGPGKIQKIPRENAYLTKDLTQDCL... | Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. Also displays broad nucleoside diphosphate kinase activity. Involved in mainta... | Q96M32 |
Q97QC4 | CRCB2_STRPN | Putative fluoride ion transporter CrcB 2 | Streptococcus | MKKEQFYPLGIFLAAMLGGLVRYLVSTWLPASPDFPWGTLFVNYLGIFCLIYLVKGYLVYKGTSKGLILALGTGFCGGLTTFSSLMLDTVKLLDTGRYLSLILYLLLSIGGGLLLAYYLGRKKW | Important for reducing fluoride concentration in the cell, thus reducing its toxicity. | Q97QC4 |
Q6LUJ8 | FTSH_PHOPR | ATP-dependent zinc metalloprotease FtsH | Photobacterium | MWLQVTNCSTLHSSLSYCGANTLSDMAKNLILWLVIAVVLMSVFQSFGPSDSAGRQVDYTTFVREIGQDQIREARFNEREITVFKRDNTRYVTYLPVFNDQKLLDDLINANVKVLGTPPEEPSLLASIFISWFPMLLLIGVWVFFMRQMQGGGGGKGAMSFGKSKARMMSEDQIKTTFADVAGCDEAKEDVKELVDYLRDPSRFQKLGGKIPTGILLVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGVGGGHDEREQTLNQMLVEMDGFEGNEGVIV... | Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. | Q6LUJ8 |
A9MU86 | OTSA_SALPB | UDP-glucose-glucosephosphate glucosyltransferase | Salmonella | MSRLVVVSNRIAPPDNKGGAGGLAVGVLGALKAAGGLWFGWSGETGNEDEPLKKVTKGNITWASFNLSEQDYEDYYCQFSNAVLWPAFHYRLDLVQFQRPAWEGYMRVNALLADKLLPLIKENDIIWVHDYHLLPFASELRKRGVNNRIGFFLHIPFPTPEIFNALPPHDELLEQLCDFDLLGFQTENDRLAFLDSLSSQTRVTTRSGKQHIAWGKDFQTEVYPIGIEPDEIALQAAGPLPPKLAQLKAELKNVKNIFSVERLDYSKGLPERFLAYEALLENYPQHRGKIRYTQIAPTSRGEVQAYQDIRHQLETEAGRI... | Probably involved in the osmoprotection via the biosynthesis of trehalose. Catalyzes the transfer of glucose from UDP-alpha-D-glucose (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose-6-phosphate. Acts with retention of the anomeric configuration of the UDP-sugar donor. | A9MU86 |
Q8TWR5 | IF2B_METKA | eIF-2-beta | Methanopyrus | MVEYDYEELLERAYEQLPEEVLEDRRFEMPKPKVSVEGKTTVIRNFKEISKKLDRDPEHITKYFLKELGTAGHVDGGRLILHGVYHPKLVEEELKNYVEEFVLCPECGKPDTKLVREDRQWILKCEACGAWSSVRRLK | eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. | Q8TWR5 |
B0R9H2 | TH11_HALS3 | Probable transposase for insertion sequence element ISH11 | Halobacterium | MSPATLQDDPSVDSFFNVVETETLALFEHLSFEFLEEFDVFAPAETGRTRDHEPPELMRGFLHCYYKDIYGIRPVERELRNTVVWLSCGFDRPPSRDAVDRFLTDLEHVVNKVFDHLVEQAALRGLLDLTYCIDSTDVRAMPADQDASKCYDPTDDEYYHGYGCTIVSTGQKIPIAAEFTESKQAPEETAMRVTRDALAVAKPIWMVGDSAYDTLDWHDHLLAAGVVPVAPYNARNTDDPKDIEYRVEDRIEQHSEDVQLKQSTLDETYNRRTGVERTNESVKDCGLGRTHARGRVHARAQVFLALCLRLVVAITNYERG... | Involved in the transposition of the insertion sequence ISH11. | B0R9H2 |
B8D9H0 | RL21_BUCA5 | 50S ribosomal protein L21 | Buchnera | MYAVFISGGKQYRVVKNQIIRLEKLNSPLGTTIEFDKILMLFDKDSIKIGTPFVEGGTIKAHIQNHGRLKKIKIIKFNRRKHYKKQQGHRQYFTDVKIIDINSIKGEV | This protein binds to 23S rRNA in the presence of protein L20. | B8D9H0 |
C5C9T9 | RS15_MICLC | 30S ribosomal protein S15 | Micrococcus | MALDPAVKQQIIKEYATHEGDTGSPEVQIAVLSRRIKDLTEHLKEHKHDHHTRRGLMGLVGRRRRMLGYLQNVDIERYRALIERLGLRK | Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. | C5C9T9 |
Q11I83 | ILVC_CHESB | Ketol-acid reductoisomerase type I | unclassified Chelativorans | MRVYYDRDADLNLIKSKKVAIIGYGSQGRAHALNLKDSGAKDLAVALRPGSASAKKAEADGLKVMSVAEAAGWADLMMMATPDELQAGIYNNEIAPNIRDGAAIAFAHGLNVHFGLIEPKKTVDVLMIAPKGPGHTVRSEYQRGGGVPCLVAVHHDASGNALDLALSYACGVGGGRSGIIETTFREECETDLFGEQVVLCGGLVELIRAGFETLVEAGYAPEMAYFECLHEVKLIVDLIYEGGIANMNYSISNTAEWGEYVSGPRIITPETKAEMKRVLKDIQTGKFTAEWMQEWHSGAARFKATRRLNDSHQIEEVGEK... | Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobu... | Q11I83 |
A8AN88 | UBIA_CITK8 | 4-HB polyprenyltransferase | Citrobacter | MEWSLTQNKLLAFHRLMRTDKPIGALLLLWPTLWALWVATPGVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRPLPSGAVTEKEARTLFVVLVALSFLLVLTLNTMTILLSIAALALAWVYPFMKRYTHLPQVVLGAAFGWSIPMAFAAVSESVPLSCWLMFLANILWAVAYDTQYAMVDRDDDLKIGIKSTAILFGRHDKLIIGILQIAVLALMALIGWLNGLGWGYYWSVLVAGALFVYQQKLIVGREREACFKAFMNNNYVGLVLFLGLAMSYVG | Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-... | A8AN88 |
D2Y297 | H1624_CYRHA | Peptide F4-19.87 | Haplopelma | MNTVRVTFLLVFVLAVSLGQADKDENRMEMQEKTEQGRSYLDFAENLLLQKLEELEAKLLEEDSEESRNSRQKRCIGEGVPCDENDPRCCSGLVCLKPTLHGIWYKSYYCYKK | Probable ion channel inhibitor. | D2Y297 |
A5EDB2 | UREG1_BRASB | Urease accessory protein UreG 1 | unclassified Bradyrhizobium | MLHALRQAKAQATATVAARVGIGGPVGSGKTALIEALIPVLQRRGVDFAVVTNDLVTKEDAERLRRSGLIDPDRVSAVEAGACPHTVIREDPTLNIAAGDELEARFPGVELILFESGGDNLASTFSLDLVDWWIFVIDVAGGDDIPRKRGPGLLRCDLLVVNKIDLAPHVGVDLDRMLADARQVRGGKPVIATNLKAGTGVEAVADAISAAVLFRI | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | A5EDB2 |
Q818P5 | MNTR_BACCR | Manganese transport regulator | Bacillus cereus group | MPTPSMEDYIEQIYLLIDEKGYARVSDIAEALSVHPSSVTKMVQKLDKDEYLIYEKYRGLVLTTKGKKIGERLVYRHDLLEQFMRIIGVDESKIYNDVEGIEHHLSWEAIDRIGDLVQYFEQDTVRVETLRGVQRANEEKSN | Central regulator of manganese homeostasis. | Q818P5 |
A8FKR5 | RS12_CAMJ8 | 30S ribosomal protein S12 | Campylobacter | MPTINQLVRKERKKVLEKSKSPALKNCPQRRGVCTRVYTTTPKKPNSALRKVAKVRLTSGFEVISYIGGEGHNLQEHSIVLVRGGRVKDLPGVKYHIVRGALDTAGVAKRTVSRSKYGAKRPKAGTAK | Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The com... | A8FKR5 |
B1ZWN7 | ATPG_OPITP | F-ATPase gamma subunit | Opitutus | MASTRDIRRRIKSVKNTRQITKAMELVAASKMKKAQQAAVAGRPYAELMAQMLATLGDRVEEAQHPFLVQREVKTRGIILITTDKGLAGPLNANLFKLVTDIQSPAKYVVVGRKGAQFIARTRRDLLAEFQVSDRAAFAEVKVVVEFMTKQFIDGVVDSVEVIWPRFKNTLVQIPTIAQLLPLRGVQHAVESLQHGTGVSAPRSPAVEAQMLFEPDPVSVLSALLPLYINREVYHQVLDAKASEHSARMVAMKTAKDNATKLLDDLTLEYNKARQAGITQEIIEIAAAQFAAAS | Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | B1ZWN7 |
A4QJZ9 | PSBA_ARAHI | Photosystem II Q(B) protein | Arabis | MTAILERRESESLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADI... | Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photoni... | A4QJZ9 |
B6HV34 | ADRF_PENRW | Andrastin A biosynthesis cluster protein F | Penicillium chrysogenum species complex | MSLLQDIVLIITGSASGIGLATATAALSQGAKILGVDVSWAPVSLTEHASYKFIQANLTHEATPKQVVETCIKEFGRIDGLLNIAGIMDQNSSVDSLTDDMWERCIAINLTAPVKLMREVIPIMRQQKSGSIVNVGSKAATSGAASGVAYTASKHGLMGATKNVAWRYKQEGIRCNAVCPGGVPTGIVQASDPTTWDKDALATMSHIHQAHAADRQEGLGVEAEDIANCLLFLVSSQSKRINGAIIPVDNAWSVI | Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (Ref.2). The first step of the pathway is the synthesis of 3,5-di... | B6HV34 |
Q0W1L9 | THIM_METAR | 4-methyl-5-beta-hydroxyethylthiazole kinase | Methanocella | MDARSLSGILTEVREKRPLVHHITNYVTVNDCANVTLCIGAAPVMAHAHDEVAEMVAMAGALVLNIGTLDHRQVESMLAAGHRANELNIPIILDPVGAGATRLRTETAKTLLHKLHVSVLKGNAGEIATLAGAEGKVRGVDSAGVSGDPAEFARGLAEKLGLVVAVSGATDIVTDGKRLIYVDNGHEMMGKLSGTGCMASSISGAFAAASKDYVTSTAAALASFGVAGEKAAKRCEGPASFKIALLDEIYRLTADEVAHNIKVRFA | Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ). | Q0W1L9 |
B1JFW2 | NANK_YERPY | N-acetyl-D-mannosamine kinase | Yersinia | MGKGLALDIGGTKIAAAVVTESGMLIGRQQIATPRGGAGQLAAALETLIAPYRHQVDFIAVASTGIISGGRLTALNPANLGGLADFPLYDCIRSISDLPCVLLNDGQAAAWAEYQALGDKNDNMMFVTVSTGVGGGIILNKKLLVGQRGLAGHIGHTLSDPHGVLCGCGRRGCVESVASGTAIGAETLGWKQPVSAATVFDMAQQGDAQAGKVINRSAAAIAQMLADMKMALDLEVVILGGSVGLAVGYLERVVAAQKTLPGIYRVPVQEAHHRQDSGLLGAALWARASL | Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. | B1JFW2 |
P53938 | EOS1_YEAST | ER-localized and oxidants sensitive protein 1 | Saccharomyces | MTWILSTGMGPHEDKYAKHERATFKKTYSSMKTLSLNHLTAKQHMLMALCRDISLLPPLTYIFTSLRKAWRVSMRTSITLYEPQSLRDAFTYFWQKLNSAYDNNSSFEGASQKAVNGDGKDSLLLSALTTARASEYLLCSLWCLVSLYLSYAILDSLMVRWIVKYSTVAAILRMFSMSLIIVTLELLLLSSLSPELDYFLHTWILISCVLTAVYIWQSYLTSDLRYIRNQEGEVQEDTNVPEETEDYEDGEDDADEDSHVVVADESTVDVPSNDSLSDNSDGGLFPVNRPSVSHSQSPKRPKKYPKKAFNFTTKRTIDLY... | Involved in oxidative stress resistance and N-glycosylation. | P53938 |
P56168 | MT21_BRAJU | Metallothionein-like protein type 2, MT2-4/MT2-25 | Brassica | MSCCGGNCGCGSGCKCVGCGGCKMYPDLSFSGETTTTETLVLGVAPAMNSQFEASGETFVAENDACKCGSDCKCNPCTCK | Metallothioneins have a high content of cysteine residues that bind various heavy metals. | P56168 |
Q6LWZ4 | MTRE_METMP | N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit E | Methanococcus | MDPTLISLGALALAGAAATVSGCAEDLESDVGSQSNPNSQVQLGPQMGNIHRYFNKAISGEPVSYGLYVAVAGTIAWALINAGLNVVLAIIVGAGVAAIVHGAYSVSAFLGRTVGQSKKFGQPVYMDVLTSHIGPIVGHGFIAVFTMTLAAYLATTALGNPFPLPLVSLIFGITVGAIGSSTGDVHYGAEREYQKYPFGGGIPVANQGDIDIYAEYGVRNGLDSSYFCSRFGGPLTGLCFGLIIFLDGWRSILGNIIGGDLVTKTSIALLVGLLVVAVAAVINRKLEVYARNKYGPYRN | Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. | Q6LWZ4 |
O82213 | VAP31_ARATH | Vesicle-associated protein 3-1, N-terminally processed | Arabidopsis | MSNNELLEIEPMYLQFPFELKKQMSCSLYLTNKTDNNVAFKVKTTNRNNYCVRPNYGLILPKSTCKVLVTMQAQKEVPSDMQSFEKFMIQSVLASPGVTAKEVTREMFSKESGHVVEETKLRVTYVCSTTTNITSSPRTRRGFIFQCFC | May play a role in vesicle trafficking. | O82213 |
Q7Z4L9 | PPR42_HUMAN | Leucine-rich repeat-containing protein 67 | Homo | MVRLTLDLIARNSNLKPRKEETISQCLKKITHINFSDKNIDAIEDLSLCKNLSVLYLYDNCISQITNLNYATNLTHLYLQNNCISCIENLRSLKKLEKLYLGGNYIAVIEGLEGLGELRELHVENQRLPLGEKLLFDPRTLHSLAKSLCILNISNNNIDDITDLELLENLNQLIAVDNQLLHVKDLEFLLNKLMKLWKIDLNGNPVCLKPKYRDRLILVSKSLEFLDGKEIKNIERQFLMNWKASKDAKKISKKRSSKNEDASNSLISNFKTMHHIVPVYYPQVGKPKLAFFSEIQRYPVNANASPESS | Regulates phosphatase activity of protein phosphatase 1 (PP1) complexes in the testis. | Q7Z4L9 |
Q7VN63 | TATA_HAEDU | Sec-independent protein translocase protein TatA | Haemophilus | MGGISIWQLLIIVAIIVLLFGTKKLRTLGTDLGESVKGFKKAMAEDKSQDANFDKVEAKESTSTTEKTKEKEQA | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. | Q7VN63 |
A3PK84 | METAA_CERS1 | Homoserine transacetylase | Cereibacter | MPITLPATLPAFDVLTHEGVMVMTPERAARQDIRPLRIGLLNLMPKKIQTENQFARLIGATPLQIDFQLIRMTEHQTKNTAAEHMEAFYRPFQEVKHEKFDGLIITGAPIEHLDFADVTYWDELCEVMDWTQTNVQSTFGVCWGGMAMIYHFHRVQKHRLQAKAFGCFRHRNVAPTSPYLRGFSDDFVIPVSRWTEMRQAEIDAAPGLRTLLASDEAGPCLVEDPGHRALYIFNHFEYDSDTLKQEYDRDVANGKPINVPANYYPDDDPSKPPLNRWRSHAHLLYGNWINEIYQSTPYDPQQIGR | Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. | A3PK84 |
A9L591 | RLMKL_SHEB9 | rRNA (guanine-N(7)-)-methyltransferase RlmK | Shewanella | MLNFFAAAPKGFEYSLAQELTEFGATEVKESVAGVYFTASLALAYRITLWTRLASRIVLVIYKGSCESAEQLYNAAYCVDWPAHFSNKSTFSIDFHGTGGFLNNTQFGALKIKDAIVDRFRDDDIERPNVSRVDAEFKVDAHFRNGVITIAMNFSGPSLHQRGYRSTTGEAPLKENLAANMLVRSGWQASPSTLLDPFCGSGTVLIEAALMAADIAPGLQRSRFGFEHWRRHDKAVWQEIVEEAKARASLGVKRCEIKFYGSDIDSRLVALAKRNAENAGVLELIEFKVADALTIAPPAESGYLITNPPYGERLGNVSEL... | Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. | A9L591 |
Q5HM28 | ECFA2_STAEQ | Energy-coupling factor transporter ATP-binding protein EcfA2 | Staphylococcus | MSIQFNQVSYIYQQGTPYEFEAIKNVSLTLEQGKYYAIIGQTGSGKSTLIQHLNALLKPTTGSVNINGLEVTNKTKDKHLRHIRKEVGIVFQFPESQLFEDSVEKEIEFGPKNFNMNLKNVKDKAFQLLLELGFSRNVMSSSPFQMSGGQMRKIAIVSILAMDPQVIILDEPTAGLDPNSKHQVMSLIKKIQIEENKTIILVSHDMDDVARYSDEVVVMNKGTIVEKSNPRNLFNQKTQLLKWHIELPKVVKLQKDIEKKYNMLFPKLAMNEEEFVKLYKEWHHEE | ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. | Q5HM28 |
Q45W87 | OL111_ARAHY | Oleosin Ara h 11.0101 | Arachis | MAEALYYGGRQRQEQPRSTQLVKATTAVVAGGSLLILAGLVLAGTVIGLTTITPLFVIFSPVLVPAVITVALLGLGFLASGGFGVAAITVLTWIYRYVTGKHPPGANQLDTARHKLMGKAREIKDFGQQQTSGAQAS | May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth. | Q45W87 |
A0A455R413 | ASCA_ACREG | Ascofuranone/ascochlorin biosynthesis clusters protein A | Acremonium | MAAKSRSPKRGTSEKTPLVEKEAPYQPPTKGILSKLPASWVPYAQLIRLEQPHGNYMIYFPHIIGLMYASAIRPTELSVLGHRAAIFAIWTFLMRGAGCAWNDNVDQDFDRKTERCRHRPIARGAISTTQGHVFTLILTLLGFAAIQSLPIECTYVGVGTTVLSAIYPFGKRFTHFAQVILGSTLASTIALSAYSVGLPALSKDYFVPTLCLSATIMLLVVFYDVVYARADTTDDLKSGVKGMAVRFRNHLEGLFAFITLSIAGSLTTLGYLVGMGHWFYLFSVGGLTFGLVSMVALTHWNILPGYSSGRCYAFAILNLL... | Prenytransferase; part of the asc-1 gene cluster that mediates the biosynthesis of both ascochlorin and ascofuranone, a strong inhibitor of cyanide-insensitive alternative oxidases and a promising drug candidate against African trypanosomiasis . The first step in the pathway is performed by the non-reducing polyketide ... | A0A455R413 |
Q65QH0 | GLPE_MANSM | Thiosulfate sulfurtransferase GlpE | Basfia | MFKEITPQQAWQLMIEENATLVDIRDEQRFTYSHAKGAFHLTGQSYGKFQIQCDFDDPVIVSCYHGISSRNVAAFLVEQGYDNIYSIIGGFEGWQRAGLPIETAY | Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. | Q65QH0 |
Q48UH5 | Y517_STRPM | Nucleotide-binding protein M28_Spy0517 | Streptococcus | MSDKHINLVIVTGMSGAGKTVAIQSFEDLGYFTIDNMPPALVPKFLELIEQTNENRRVALVVDMRSRLFFKEINSTLDSIESNPSIDFRILFLDATDGELVSRYKETRRSHPLAADGRVLDGIRLERELLSPLKSMSQHVVDTTKLTPRQLRKTISDQFSEGSNQASFRIEVMSFGFKYGLPLDADLVFDVRFLPNPYYKVELREKTGLDEDVFNYVMSHPESEVFYKHLLNLIVPILPAYQKEGKSVLTVAIGCTGGQHRSVAFAHCLAESLATDWSVNESHRDQNRRKETVNRS | Displays ATPase and GTPase activities. | Q48UH5 |
Q8A498 | IF1_BACTN | Translation initiation factor IF-1 | Bacteroides | MAKQSAIEQDGVIVEALSNAMFRVELENGHEITAHISGKMRMHYIKILPGDKVRVEMSPYDLSKGRIVFRYK | One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-... | Q8A498 |
A0A1V0QSE8 | ERIJ_HERER | Erinacine biosynthesis cluster protein J | Hericium | MSTQNYHIVAVPPNEWGHMRPMIAFLARLVAVSLNSVDITVTLIIAESAVAKARTELSIQLAGEGIQSAESRFEVVPTAVHMFWPADAYLPALKATYAEVIKKKEPDFALLESMIHPFFDVVRSSATKPIKVGAWLPVALPSWTSMAPICYIRDDPQAYVKQVETTMAEKGLGYMEAASDAYLSHVNGRVLRIPGFPEMTDYEGFPQEPPVLLPVAMVVDWVFGIRDADILVTSTAQALERQGLQVFSKWLKEQPKHSDILAVGPLTSQRTPEVARKEKEEADAGGFTAFLDAWAAKKGPKSVLYICFGSVLLPAEIEHL... | UDP-glycosyltransferase; part of the gene cluster that mediates the biosynthesis of erinacines, cyathane-xylosides that show unique biological activities, including leishmanicidal activity, stimulating activity for nerve growth-factor synthesis, and agonistic activity toward the kappa opioid receptor . The geranylgeran... | A0A1V0QSE8 |
P00296 | PLAS_SOLTU | Plastocyanin | Solanum | LDVLLGGDDGSLAFIPGNFSVSAGEKITFKNNAGFPHNVVFDEDEIPAGVDASKISMAEEDLLNAAGETYSVTLSEKGTYTFYCAPHQGAGMVGKVTVN | Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. | P00296 |
Q8Y626 | TYSY_LISMO | Thymidylate synthase | Listeria | MKQYLDLEKYVLENGTQKGDRTGTGTISTFGYQMRFDLQEGFPIMTTKRVPFKLVVSELLWFLHGDTNIRYLLQHNNNIWNEWAFERFVKSDDYKGEDMTDFGLRAERDPAFKEVYQAEMEKFKTRIIEDEAFATKYGELGNIYGKQWREWKTSQGETIDQLADLIEMIKTNPNSRRLIVSAWNPEDIPNMALPPCHSLFQFYVADGKLSCQLYQRSADIFLGVPFNIASYALLTHLIAREVGLDVGEFIHTMGDAHLYNNHIEQVKEQLSRTPHALPKLVLSDKPATIFDFEVADISLDGYNPDPSIKAPISV | Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracell... | Q8Y626 |
A4SXR0 | LEU1_POLAQ | Alpha-isopropylmalate synthase | Polynucleobacter | MSDKVIIFDTTLRDGEQSPGASMTKDEKVRIARQLERLKVDVIEAGFAASSEGDFQAISAVAAAVKDSIVCSLARANDKDITRAADALQAANAKRIHAFLATSPLHMAVKLRMSPEEVLEQAKRSIRFARNLASDIEFSAEDGYRSEMDFLCRVVEAVINEGASTINIPDTVGYATPELYGDFIKTLRTRVPNSDKAVWSVHCHNDLGMAVANSLAGVKIGGARQIECTINGLGERAGNTALEEIVMALRTRKDYFDMVCGIDASQIVPASKLVSQITGFVVQPNKAVVGANAFAHTSGIHQDGILKNRDTYEIMRAEDV... | Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). | A4SXR0 |
B8HGW7 | MRAY_PSECP | UDP-MurNAc-pentapeptide phosphotransferase | Pseudarthrobacter | MIALLIGAGLALLCALVGTPLFIRLLVRRGYGQFIRDDGPTSHHTKRGTPTMGGTVVVAAVLLSYGLTHLIMFLMNPDSPGPSASALILLFLMVGMGLVGFLDDFIKISRQRSLGLNAKAKLILQAAVGVIFAVLALNFPDESGLAPASTKISLVRDLPWLDLAFGGTVLGAILFVVWSNLIVTAATNGVNLTDGLDGLAAGASVMVFGAYTLMGIWQSNQACGSPREAGSGCYSVRDPLDLALLAAIMSAALVGFLWWNTSPAKIFMGDTGSLAIGGAIAGFAILSRTELLLGIIGGLFVLITLSVIIQVGYFKATGGK... | Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I... | B8HGW7 |
P39076 | TCPB_YEAST | CCT-beta | Saccharomyces | MSVQIFGDQVTEERAENARLSAFVGAIAVGDLVKSTLGPKGMDKLLQSASSNTCMVTNDGATILKSIPLDNPAAKVLVNISKVQDDEVGDGTTSVTVLSAELLREAEKLIDQSKIHPQTIIEGYRLASAAALDALTKAAVDNSHDKTMFREDLIHIAKTTLSSKILSQDKDHFAELATNAILRLKGSTNLEHIQIIKILGGKLSDSFLDEGFILAKKFGNNQPKRIENAKILIANTTLDTDKVKIFGTKFKVDSTAKLAQLEKAEREKMKNKIAKISKFGINTFINRQLIYDYPEQLFTDLGINSIEHADFEGVERLALV... | Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. | P39076 |
A8GPF2 | EFTU_RICAH | Elongation factor Tu | spotted fever group | MAKAKFERTKPHVNIGTIGHVDHGKTSLTAAITTVLAKTGGAKATAYDQIDAAPEEKERGITISTAHVEYETKNRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSAADGPMLQTREHILLAKQVGVPAMVVFLNKVDVVDDPALLELVEMEVRDLLLQYGFPAYEVPIIKGSALQALAGKPEGEKAINELMDAVDNYIPHPVRATDKPFLMPIEDVFSISGRGTVVTGRVESGIIKVGEEVEIVGLKETQKTTCTGVEMFRKLLDEGQAGDNVGILLRGTKREEVERGQVLAKPGSIKPHDQFEAEVYVLSKEEGGRH... | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | A8GPF2 |
Q8FHG6 | GADC_ECOL6 | Glutamate/gamma-aminobutyrate antiporter | Escherichia | MATSVQTGKAKQLTLLGFFAITASMVMAVYEYPTFATSGFSLVFFLLLGGILWFIPVGLCAAEMATVDGWEEGGVFAWVSNTLGPRWGFAAISFGYLQIAIGFIPMLYFVLGALSYILKWPALNEDPITKTIAALIILWALALTQFGGTKYTARIAKVGFFAGILLPAFILIALAAIYLHSGAPVAIEMDSKTFFPDFSKVGTLVVFVAFILSYMGVEASATHVNEMSNPGRDYPLAMLLLMVAAICLSSVGGLSIAMVIPGNEINLSAGVMQTFTVLMSHVAPEIEWTVRVISALLLLGVLAEIASWIVGPSRGMYVTA... | Involved in glutaminase-dependent acid resistance. Exchanges extracellular glutamate (Glu) for intracellular gamma-aminobutyric acid (GABA) under acidic conditions. The ability to survive the extremely acidic conditions of the stomach is essential for successful colonization of the host by commensal and pathogenic bact... | Q8FHG6 |
Q26516 | PPIE_SCHJA | Rotamase E | Schistosoma | EDVSDDEMRTKKQKRNLPRVFFDIRIGNADRGRIVMELRSDIVPRTAENFRALCTGDRGFGYHNCCFHRVIPQFMCQGGDFVKGDGTGGKSIYGRKFDDENFQLRHEGFGVLSMANSGPNTNGSQFFICTTKCDWLDGKHVVFGRVVDGQNVVKKMESVGSKSGKVKEPVTISRCGELI | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | Q26516 |
O19015 | BGAL_FELCA | Acid beta-galactosidase | Felis | MDFPGAARLLSLLLVPLLLGPARGLRNASQRTFKIDYGHNRFLKDGQPFRYISGSIHYFRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPQPGQYQFSGEHDVEYFLKLAHELGLLVILRPGPYICAEWDMGGLPAWLLLKESIILRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPIITVQVENEYGSYFTCDYDYLRFLQRRFRDHLGGDVLLFTTDGAHEKFLQCGALQGIYATVDFGPDANITAAFQIQRKSEPRGPLVNSEFYTGWLDHWGQPHSRVRTEVVASSLHDVLAHGANVNLYMFIGGTNFAYWNG... | Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. | O19015 |
Q9GLM4 | TENS1_BOVIN | Tensin-1 | Bos | MSTSRTTEDSCELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKICSVCKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADHALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPVYTSGIYNVQGDSQTSICITIEPGLLLKGDILLKCYHKKFRSPARDVIFRVQFHTCAIHDLGVVFGKEDLDDAFKDDRFPEYGKVEFVFSYGPEKIQGMEHLENG... | Involved in fibrillar adhesion formation. May be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. | Q9GLM4 |
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